The amino acid sequence of the D-galactose-binding protein from Escherichia coli B/r

The complete primary structure of the Escherichia coli B/r galactose-binding protein was determined by the automated sequencing of fragments produced by cleavage with cyanogen bromide, o-iodosobenzoic acid, limited trypsin digestion, mild acid hydrolysis, and Staphylococcus aureus strain V8 protease...

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Bibliographic Details
Published inThe Journal of biological chemistry Vol. 256; no. 9; pp. 4350 - 4356
Main Authors Mahoney, W C, Hogg, R W, Hermodson, M A
Format Journal Article
LanguageEnglish
Published United States American Society for Biochemistry and Molecular Biology 10.05.1981
Subjects
Amino Acid Sequence
Calcium-Binding Proteins
Carboxypeptidase B
Carboxypeptidases
Carrier Proteins
Cyanogen Bromide
Escherichia coli
Escherichia coli - analysis
Galactose
galactose-binding protein
Monosaccharide Transport Proteins
Peptide Fragments - analysis
Periplasmic Binding Proteins
proteins
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Summary:The complete primary structure of the Escherichia coli B/r galactose-binding protein was determined by the automated sequencing of fragments produced by cleavage with cyanogen bromide, o-iodosobenzoic acid, limited trypsin digestion, mild acid hydrolysis, and Staphylococcus aureus strain V8 protease. The protein, which has 309 amino acids, is notable in the extent to which it differs from the L-arabinose-binding protein. Comparison of these two proteins indicates only about 18% homology despite the close structural resemblence of the molecules which they bind. The galactose-binding protein is the chemoreceptor initiating chemotaxis toward galactose, and it thus becomes the first protein component required for chemotaxis for which the primary structure is known. GM 24602
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)69441-X